LAMA3_HUMAN
ID LAMA3_HUMAN Reviewed; 3333 AA.
AC Q16787; B0YJ33; Q13679; Q13680; Q6VU67; Q6VU68; Q6VU69; Q76E14; Q96TG0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Laminin subunit alpha-3;
DE AltName: Full=Epiligrin 170 kDa subunit;
DE Short=E170;
DE AltName: Full=Epiligrin subunit alpha;
DE AltName: Full=Kalinin subunit alpha;
DE AltName: Full=Laminin-5 subunit alpha;
DE AltName: Full=Laminin-6 subunit alpha;
DE AltName: Full=Laminin-7 subunit alpha;
DE AltName: Full=Nicein subunit alpha;
DE Flags: Precursor;
GN Name=LAMA3; Synonyms=LAMNA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), DISEASE, AND VARIANT
RP SER-2834.
RX PubMed=12915477; DOI=10.1093/hmg/ddg234;
RA McLean W.H.I., Irvine A.D., Hamill K.J., Whittock N.V.,
RA Coleman-Campbell C.M., Mellerio J.E., Ashton G.S.,
RA Dopping-Hepenstal P.J.H., Eady R.A.J., Jamil T., Phillips R.J.,
RA Shabbir S.G., Haroon T.S., Khurshid K., Moore J.E., Page B., Darling J.,
RA Atherton D.J., Van Steensel M.A.M., Munro C.S., Smith F.J.D., McGrath J.A.;
RT "An unusual N-terminal deletion of the laminin alpha3a isoform leads to the
RT chronic granulation tissue disorder laryngo-onycho-cutaneous syndrome.";
RL Hum. Mol. Genet. 12:2395-2409(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RX PubMed=15044476; DOI=10.1074/jbc.m400670200;
RA Kariya Y., Yasuda C., Nakashima Y., Ishida K., Tsubota Y., Miyazaki K.;
RT "Characterization of laminin 5B and NH2-terminal proteolytic fragment of
RT its alpha3B chain: promotion of cellular adhesion, migration, and
RT proliferation.";
RL J. Biol. Chem. 279:24774-24784(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Stockwell T.B., Busam D.A., Ferriera S.M., Brownley A.N., Strausberg R.L.,
RA Kirkness E.F., Rogers Y.-H., Levy S.;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-2834.
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-2858 (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [MRNA] OF 1528-2858 (ISOFORMS 1/2), AND INVOLVEMENT IN JEB2B.
RC TISSUE=Keratinocyte;
RX PubMed=8586427; DOI=10.1006/geno.1995.9877;
RA Vidal F., Baudoin C., Miquel C., Galliano M.-F., Christiano A.M., Uitto J.,
RA Ortonne J.-P., Meneguzzi G.;
RT "Cloning of the laminin alpha 3 chain gene (LAMA3) and identification of a
RT homozygous deletion in a patient with Herlitz junctional epidermolysis
RT bullosa.";
RL Genomics 30:273-280(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1528-3333 (ISOFORMS 1/2).
RA Aberdam D., Vidal F., Baudoin C., Miquel C., Ortonne J.-P., Meneguzzi G.;
RT "Mutation in LAMA3 gene in a patient affected by H-Jeb.";
RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Keratinocyte;
RX PubMed=8077230; DOI=10.1016/s0021-9258(17)31713-1;
RA Ryan M.C., Tizard R., Vandevanter D.R., Carter W.G.;
RT "Cloning of the LamA3 gene encoding the alpha 3 chain of the adhesive
RT ligand epiligrin. Expression in wound repair.";
RL J. Biol. Chem. 269:22779-22787(1994).
RN [8]
RP INVOLVEMENT IN JEB2B, AND VARIANT JEB2B 2270-ARG--GLN-3333 DEL.
RX PubMed=8530087; DOI=10.1006/geno.1995.1246;
RA McGrath J.A., Kivirikko S., Ciatti S., Moss C., Dunnill G.S., Eady R.A.,
RA Rodeck C.H., Christiano A.M., Uitto J.;
RT "A homozygous nonsense mutation in the alpha 3 chain gene of laminin 5
RT (LAMA3) in Herlitz junctional epidermolysis bullosa: prenatal exclusion in
RT a fetus at risk.";
RL Genomics 29:282-284(1995).
RN [9]
RP INVOLVEMENT IN JEB2B, AND VARIANT JEB2B 2270-ARG--GLN-3333 DEL.
RX PubMed=7633458; DOI=10.1093/hmg/4.5.959;
RA Kivirikko S., McGrath J.A., Baudoin C., Aberdam D., Ciatti S.,
RA Dunnill M.G., McMillan J.R., Eady R.A., Ortonne J.P., Meneguzzi G.;
RT "A homozygous nonsense mutation in the alpha 3 chain gene of laminin 5
RT (LAMA3) in lethal (Herlitz) junctional epidermolysis bullosa.";
RL Hum. Mol. Genet. 4:959-962(1995).
RN [10]
RP INVOLVEMENT IN JEB2A, AND INVOLVEMENT IN JEB2B.
RX PubMed=11810295; DOI=10.1007/s00439-001-0630-1;
RA Nakano A., Chao S.C., Pulkkinen L., Murrell D., Bruckner-Tuderman L.,
RA Pfendner E., Uitto J.;
RT "Laminin 5 mutations in junctional epidermolysis bullosa: molecular basis
RT of Herlitz vs. non-Herlitz phenotypes.";
RL Hum. Genet. 110:41-51(2002).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Binding to cells via a high affinity receptor, laminin is
CC thought to mediate the attachment, migration and organization of cells
CC into tissues during embryonic development by interacting with other
CC extracellular matrix components.
CC -!- FUNCTION: Laminin-5 is thought to be involved in (1) cell adhesion via
CC integrin alpha-3/beta-1 in focal adhesion and integrin alpha-6/beta-4
CC in hemidesmosomes, (2) signal transduction via tyrosine phosphorylation
CC of pp125-FAK and p80, (3) differentiation of keratinocytes.
CC -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three
CC different polypeptide chains (alpha, beta, gamma), which are bound to
CC each other by disulfide bonds into a cross-shaped molecule comprising
CC one long and three short arms with globules at each end. Alpha-3 is a
CC subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein),
CC laminin-6 (laminin-311 or K-laminin) and laminin-7 (laminin-321 or KS-
CC laminin).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane. Note=Major component.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=2; Synonyms=B;
CC IsoId=Q16787-2; Sequence=Displayed;
CC Name=1; Synonyms=A;
CC IsoId=Q16787-1; Sequence=VSP_035738, VSP_035739;
CC Name=3;
CC IsoId=Q16787-3; Sequence=VSP_043487;
CC Name=4;
CC IsoId=Q16787-4; Sequence=VSP_047079, VSP_047080, VSP_043487;
CC -!- TISSUE SPECIFICITY: Skin; respiratory, urinary, and digestive epithelia
CC and in other specialized tissues with prominent secretory or protective
CC functions. Epithelial basement membrane, and epithelial cell tongue
CC that migrates into a wound bed. A differential and focal expression of
CC the subunit alpha-3 is observed in the CNS.
CC -!- INDUCTION: Laminin-5 is up-regulated in wound sites of human skin.
CC -!- DOMAIN: The alpha-helical domains I and II are thought to interact with
CC other laminin chains to form a coiled coil structure.
CC -!- DOMAIN: Domain G is globular.
CC -!- DISEASE: Epidermolysis bullosa, junctional 2A, intermediate (JEB2A)
CC [MIM:619783]: A form of epidermolysis bullosa, a genodermatosis
CC characterized by recurrent blistering, fragility of the skin and
CC mucosal epithelia, and erosions caused by minor mechanical trauma.
CC JEB2A is an autosomal recessive, intermediate form in which blistering
CC lesions occur between the epidermis and the dermis at the lamina lucida
CC level of the basement membrane zone. In intermediate forms of
CC junctional epidermolysis bullosa, blistering does not lead to the
CC formation of chronic granulation tissue and does not affect the
CC lifespan of affected individuals. Nail dystrophy and dental enamel
CC defects are present. Scarring or non-scarring alopecia and diffuse hair
CC loss may occur. {ECO:0000269|PubMed:11810295}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Epidermolysis bullosa, junctional 2B, severe (JEB2B)
CC [MIM:619784]: A form of epidermolysis bullosa, a genodermatosis
CC characterized by recurrent blistering, fragility of the skin and
CC mucosal epithelia, and erosions caused by minor mechanical trauma.
CC JEB2B is an autosomal recessive form in which blistering lesions occur
CC between the epidermis and the dermis at the lamina lucida level of the
CC basement membrane zone. It belongs to the severe spectrum of junctional
CC epidermolysis bullosa (previously known as generalized severe or
CC Herlitz type), characterized by onset of blistering over large regions
CC of the body at birth or in early infancy. Blistering also affects the
CC mucous membranes, such as the moist lining of the mouth and digestive
CC tract, which can make it difficult to eat and digest food. The
CC extensive blistering leads to scarring and the formation of red, bumpy
CC patches called granulation tissue. Other complications can include
CC fusion of the fingers and toes, abnormalities of the fingernails and
CC toenails, joint deformities, dental enamel defects, and alopecia.
CC Severe, junctional forms are associated with death in the first 6 to 24
CC months of life. {ECO:0000269|PubMed:7633458,
CC ECO:0000269|PubMed:8530087, ECO:0000269|PubMed:8586427}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Laryngoonychocutaneous syndrome (LOCS) [MIM:245660]: Autosomal
CC recessive epithelial disorder confined to the Punjabi Muslim
CC population. The condition is characterized by cutaneous erosions, nail
CC dystrophy and exuberant vascular granulation tissue in certain
CC epithelia, especially conjunctiva and larynx.
CC {ECO:0000269|PubMed:12915477}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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DR EMBL; AY327114; AAQ72569.1; -; mRNA.
DR EMBL; AY327115; AAQ72570.1; -; mRNA.
DR EMBL; AY327116; AAQ72571.1; -; mRNA.
DR EMBL; AB107369; BAD13428.1; -; Genomic_DNA.
DR EMBL; EF444992; ACA06011.1; -; Genomic_DNA.
DR EMBL; AC010754; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC067796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X85107; CAA59428.1; -; mRNA.
DR EMBL; X85108; CAA59429.1; -; mRNA.
DR EMBL; X84900; CAA59325.1; -; mRNA.
DR EMBL; L34155; AAA59483.1; -; mRNA.
DR CCDS; CCDS11880.1; -. [Q16787-1]
DR CCDS; CCDS42419.1; -. [Q16787-2]
DR CCDS; CCDS45838.1; -. [Q16787-3]
DR CCDS; CCDS59307.1; -. [Q16787-4]
DR PIR; A55347; A55347.
DR RefSeq; NP_000218.3; NM_000227.4.
DR RefSeq; NP_001121189.2; NM_001127717.2.
DR RefSeq; NP_001121190.2; NM_001127718.2.
DR RefSeq; NP_001289925.1; NM_001302996.1.
DR RefSeq; NP_937762.2; NM_198129.2.
DR BioGRID; 110103; 48.
DR ComplexPortal; CPX-1774; Laminin-332 complex variant A. [Q16787-1]
DR ComplexPortal; CPX-1775; Laminin-311 complex variant A. [Q16787-1]
DR ComplexPortal; CPX-1776; Laminin-321 complex. [Q16787-1]
DR ComplexPortal; CPX-3165; Laminin-332 complex variant B. [Q16787-2]
DR ComplexPortal; CPX-3166; Laminin-311 complex variant B. [Q16787-2]
DR CORUM; Q16787; -.
DR IntAct; Q16787; 16.
DR MINT; Q16787; -.
DR STRING; 9606.ENSP00000324532; -.
DR ChEMBL; CHEMBL2364187; -.
DR DrugBank; DB06245; Lanoteplase.
DR GlyGen; Q16787; 6 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q16787; -.
DR PhosphoSitePlus; Q16787; -.
DR SwissPalm; Q16787; -.
DR BioMuta; LAMA3; -.
DR DMDM; 215274012; -.
DR EPD; Q16787; -.
DR jPOST; Q16787; -.
DR MassIVE; Q16787; -.
DR MaxQB; Q16787; -.
DR PaxDb; Q16787; -.
DR PeptideAtlas; Q16787; -.
DR PRIDE; Q16787; -.
DR ProteomicsDB; 2880; -.
DR ProteomicsDB; 61068; -. [Q16787-2]
DR ProteomicsDB; 61069; -. [Q16787-1]
DR ProteomicsDB; 61070; -. [Q16787-3]
DR Antibodypedia; 1948; 191 antibodies from 30 providers.
DR DNASU; 3909; -.
DR Ensembl; ENST00000269217.11; ENSP00000269217.5; ENSG00000053747.17. [Q16787-1]
DR Ensembl; ENST00000313654.14; ENSP00000324532.8; ENSG00000053747.17. [Q16787-2]
DR Ensembl; ENST00000399516.7; ENSP00000382432.2; ENSG00000053747.17. [Q16787-3]
DR Ensembl; ENST00000587184.5; ENSP00000466557.1; ENSG00000053747.17. [Q16787-4]
DR GeneID; 3909; -.
DR KEGG; hsa:3909; -.
DR MANE-Select; ENST00000313654.14; ENSP00000324532.8; NM_198129.4; NP_937762.2.
DR UCSC; uc002kuq.4; human. [Q16787-2]
DR CTD; 3909; -.
DR DisGeNET; 3909; -.
DR GeneCards; LAMA3; -.
DR GeneReviews; LAMA3; -.
DR HGNC; HGNC:6483; LAMA3.
DR HPA; ENSG00000053747; Low tissue specificity.
DR MalaCards; LAMA3; -.
DR MIM; 226700; phenotype.
DR MIM; 245660; phenotype.
DR MIM; 600805; gene.
DR MIM; 619783; phenotype.
DR MIM; 619784; phenotype.
DR neXtProt; NX_Q16787; -.
DR OpenTargets; ENSG00000053747; -.
DR Orphanet; 79402; Intermediate generalized junctional epidermolysis bullosa.
DR Orphanet; 2407; Laryngo-onycho-cutaneous syndrome.
DR Orphanet; 79404; Severe generalized junctional epidermolysis bullosa.
DR PharmGKB; PA30272; -.
DR VEuPathDB; HostDB:ENSG00000053747; -.
DR eggNOG; KOG1836; Eukaryota.
DR GeneTree; ENSGT00940000155638; -.
DR InParanoid; Q16787; -.
DR OrthoDB; 2342at2759; -.
DR PhylomeDB; Q16787; -.
DR TreeFam; TF335359; -.
DR PathwayCommons; Q16787; -.
DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-HSA-2214320; Anchoring fibril formation.
DR Reactome; R-HSA-3000157; Laminin interactions.
DR Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR Reactome; R-HSA-446107; Type I hemidesmosome assembly.
DR Reactome; R-HSA-8874081; MET activates PTK2 signaling.
DR SignaLink; Q16787; -.
DR SIGNOR; Q16787; -.
DR BioGRID-ORCS; 3909; 20 hits in 1078 CRISPR screens.
DR ChiTaRS; LAMA3; human.
DR GeneWiki; Laminin,_alpha_3; -.
DR GenomeRNAi; 3909; -.
DR Pharos; Q16787; Tbio.
DR PRO; PR:Q16787; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q16787; protein.
DR Bgee; ENSG00000053747; Expressed in right lung and 155 other tissues.
DR ExpressionAtlas; Q16787; baseline and differential.
DR Genevisible; Q16787; HS.
DR GO; GO:0005912; C:adherens junction; IEA:Ensembl.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0030056; C:hemidesmosome; IEA:Ensembl.
DR GO; GO:0005608; C:laminin-3 complex; IEA:Ensembl.
DR GO; GO:0005610; C:laminin-5 complex; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; NAS:ProtInc.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB.
DR GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR GO; GO:0031581; P:hemidesmosome assembly; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; IBA:GO_Central.
DR GO; GO:0030155; P:regulation of cell adhesion; IEA:InterPro.
DR GO; GO:0030334; P:regulation of cell migration; IEA:InterPro.
DR GO; GO:0045995; P:regulation of embryonic development; IEA:InterPro.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 14.
DR CDD; cd00110; LamG; 5.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR009254; Laminin_aI.
DR InterPro; IPR010307; Laminin_dom_II.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF00053; Laminin_EGF; 12.
DR Pfam; PF00054; Laminin_G_1; 1.
DR Pfam; PF02210; Laminin_G_2; 4.
DR Pfam; PF06008; Laminin_I; 1.
DR Pfam; PF06009; Laminin_II; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00180; EGF_Lam; 14.
DR SMART; SM00281; LamB; 1.
DR SMART; SM00282; LamG; 5.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF49899; SSF49899; 5.
DR PROSITE; PS00022; EGF_1; 12.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS01248; EGF_LAM_1; 13.
DR PROSITE; PS50027; EGF_LAM_2; 14.
DR PROSITE; PS50025; LAM_G_DOMAIN; 5.
DR PROSITE; PS51115; LAMININ_IVA; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Basement membrane; Cell adhesion; Coiled coil;
KW Disease variant; Disulfide bond; Epidermolysis bullosa;
KW Extracellular matrix; Glycoprotein; Laminin EGF-like domain;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..3333
FT /note="Laminin subunit alpha-3"
FT /id="PRO_0000017058"
FT DOMAIN 43..298
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 299..355
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 356..425
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 426..469
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 491..535
FT /note="Laminin EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 536..588
FT /note="Laminin EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 590..630
FT /note="Laminin EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 631..683
FT /note="Laminin EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 684..728
FT /note="Laminin EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1266..1311
FT /note="Laminin EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1312..1355
FT /note="Laminin EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1356..1404
FT /note="Laminin EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1405..1455
FT /note="Laminin EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1476..1653
FT /note="Laminin IV type A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00458"
FT DOMAIN 1687..1733
FT /note="Laminin EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1734..1786
FT /note="Laminin EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1787..1821
FT /note="Laminin EGF-like 15; truncated"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 2390..2591
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 2598..2760
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 2767..2927
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 2986..3150
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 3157..3330
FT /note="Laminin G-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 298..728
FT /note="Domain V"
FT REGION 796..1265
FT /note="Domain IV 1 (domain IV B)"
FT REGION 1266..1465
FT /note="Domain III B"
FT REGION 1654..1821
FT /note="Domain III A"
FT REGION 1822..2389
FT /note="Domain II and I"
FT COILED 1852..1941
FT /evidence="ECO:0000255"
FT COILED 1987..2169
FT /evidence="ECO:0000255"
FT COILED 2322..2388
FT /evidence="ECO:0000255"
FT MOTIF 2278..2280
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 299..308
FT /evidence="ECO:0000250"
FT DISULFID 301..319
FT /evidence="ECO:0000250"
FT DISULFID 321..330
FT /evidence="ECO:0000250"
FT DISULFID 333..353
FT /evidence="ECO:0000250"
FT DISULFID 356..365
FT /evidence="ECO:0000250"
FT DISULFID 358..390
FT /evidence="ECO:0000250"
FT DISULFID 393..402
FT /evidence="ECO:0000250"
FT DISULFID 405..423
FT /evidence="ECO:0000250"
FT DISULFID 426..436
FT /evidence="ECO:0000250"
FT DISULFID 428..443
FT /evidence="ECO:0000250"
FT DISULFID 445..454
FT /evidence="ECO:0000250"
FT DISULFID 457..467
FT /evidence="ECO:0000250"
FT DISULFID 491..503
FT /evidence="ECO:0000250"
FT DISULFID 493..509
FT /evidence="ECO:0000250"
FT DISULFID 511..520
FT /evidence="ECO:0000250"
FT DISULFID 523..533
FT /evidence="ECO:0000250"
FT DISULFID 536..548
FT /evidence="ECO:0000250"
FT DISULFID 538..555
FT /evidence="ECO:0000250"
FT DISULFID 557..566
FT /evidence="ECO:0000250"
FT DISULFID 569..586
FT /evidence="ECO:0000250"
FT DISULFID 601..610
FT /evidence="ECO:0000250"
FT DISULFID 613..628
FT /evidence="ECO:0000250"
FT DISULFID 631..645
FT /evidence="ECO:0000250"
FT DISULFID 633..652
FT /evidence="ECO:0000250"
FT DISULFID 654..663
FT /evidence="ECO:0000250"
FT DISULFID 666..681
FT /evidence="ECO:0000250"
FT DISULFID 684..696
FT /evidence="ECO:0000250"
FT DISULFID 686..703
FT /evidence="ECO:0000250"
FT DISULFID 705..714
FT /evidence="ECO:0000250"
FT DISULFID 1266..1278
FT /evidence="ECO:0000250"
FT DISULFID 1268..1285
FT /evidence="ECO:0000250"
FT DISULFID 1287..1296
FT /evidence="ECO:0000250"
FT DISULFID 1299..1309
FT /evidence="ECO:0000250"
FT DISULFID 1312..1319
FT /evidence="ECO:0000250"
FT DISULFID 1314..1326
FT /evidence="ECO:0000250"
FT DISULFID 1328..1337
FT /evidence="ECO:0000250"
FT DISULFID 1340..1353
FT /evidence="ECO:0000250"
FT DISULFID 1356..1371
FT /evidence="ECO:0000250"
FT DISULFID 1358..1378
FT /evidence="ECO:0000250"
FT DISULFID 1380..1389
FT /evidence="ECO:0000250"
FT DISULFID 1392..1402
FT /evidence="ECO:0000250"
FT DISULFID 1405..1417
FT /evidence="ECO:0000250"
FT DISULFID 1407..1424
FT /evidence="ECO:0000250"
FT DISULFID 1426..1435
FT /evidence="ECO:0000250"
FT DISULFID 1438..1453
FT /evidence="ECO:0000250"
FT DISULFID 1687..1696
FT /evidence="ECO:0000250"
FT DISULFID 1689..1703
FT /evidence="ECO:0000250"
FT DISULFID 1706..1715
FT /evidence="ECO:0000250"
FT DISULFID 1718..1731
FT /evidence="ECO:0000250"
FT DISULFID 1734..1746
FT /evidence="ECO:0000250"
FT DISULFID 1736..1755
FT /evidence="ECO:0000250"
FT DISULFID 1757..1766
FT /evidence="ECO:0000250"
FT DISULFID 1769..1784
FT /evidence="ECO:0000250"
FT DISULFID 1822
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 1825
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 2561..2591
FT /evidence="ECO:0000250"
FT DISULFID 2737..2760
FT /evidence="ECO:0000250"
FT DISULFID 2895..2927
FT /evidence="ECO:0000250"
FT DISULFID 3127..3150
FT /evidence="ECO:0000250"
FT DISULFID 3302..3330
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..1620
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:8586427"
FT /id="VSP_035738"
FT VAR_SEQ 1..1609
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12915477"
FT /id="VSP_047079"
FT VAR_SEQ 1610..1665
FT /note="LSRLADVRIQGLYFTETQRLTLSEVGLEEASDTGSGRIALAVEICACPPAYA
FT GDSC -> MPPAVRRSACSMGWLWIFGAALGQCLGYSSQQQRVPFLQPPGQSQLQASYV
FT EFRPS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12915477"
FT /id="VSP_047080"
FT VAR_SEQ 1621..1665
FT /note="LYFTETQRLTLSEVGLEEASDTGSGRIALAVEICACPPAYAGDSC -> MPP
FT AVRRSACSMGWLWIFGAALGQCLGYSSQQQRVPFLQPPGQSQLQASYVEFRPS (in
FT isoform 1)"
FT /evidence="ECO:0000303|PubMed:8586427"
FT /id="VSP_035739"
FT VAR_SEQ 1946..2002
FT /note="ILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFGKHLREAEADKR
FT ESQLL -> M (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12915477"
FT /id="VSP_043487"
FT VARIANT 796
FT /note="T -> N (in dbSNP:rs17187262)"
FT /id="VAR_050078"
FT VARIANT 1206
FT /note="V -> A (in dbSNP:rs12457323)"
FT /id="VAR_050079"
FT VARIANT 1208
FT /note="P -> T (in dbSNP:rs17202961)"
FT /id="VAR_050080"
FT VARIANT 1774
FT /note="F -> L (in dbSNP:rs958631)"
FT /id="VAR_059444"
FT VARIANT 2270..3333
FT /note="Missing (in JEB2B)"
FT /evidence="ECO:0000269|PubMed:7633458,
FT ECO:0000269|PubMed:8530087"
FT /id="VAR_086401"
FT VARIANT 2702
FT /note="T -> A (in dbSNP:rs9952370)"
FT /id="VAR_047374"
FT VARIANT 2815
FT /note="N -> K (in dbSNP:rs1154232)"
FT /id="VAR_047375"
FT VARIANT 2834
FT /note="G -> S (in dbSNP:rs1154233)"
FT /evidence="ECO:0000269|PubMed:12915477,
FT ECO:0000269|PubMed:15044476, ECO:0000269|PubMed:16177791,
FT ECO:0000269|PubMed:8077230, ECO:0000269|Ref.6"
FT /id="VAR_059445"
FT CONFLICT 1544
FT /note="G -> A (in Ref. 5; CAA59429 and 6; CAA59325)"
FT /evidence="ECO:0000305"
FT CONFLICT 1743..1745
FT /note="ATG -> GMC (in Ref. 5; CAA59428/CAA59429)"
FT /evidence="ECO:0000305"
FT CONFLICT 2101
FT /note="M -> K (in Ref. 5; CAA59428/CAA59429)"
FT /evidence="ECO:0000305"
FT CONFLICT 2374
FT /note="R -> L (in Ref. 5; CAA59428/CAA59429)"
FT /evidence="ECO:0000305"
FT CONFLICT 2589
FT /note="E -> Q (in Ref. 5; CAA59428/CAA59429)"
FT /evidence="ECO:0000305"
FT CONFLICT 2672
FT /note="D -> A (in Ref. 5; CAA59428/CAA59429)"
FT /evidence="ECO:0000305"
FT CONFLICT 2804
FT /note="G -> A (in Ref. 5; CAA59428/CAA59429)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3333 AA; 366619 MW; 6F99AF4D4B99FCB0 CRC64;
MAAAARPRGR ALGPVLPPTP LLLLVLRVLP ACGATARDPG AAAGLSLHPT YFNLAEAARI
WATATCGERG PGEGRPQPEL YCKLVGGPTA PGSGHTIQGQ FCDYCNSEDP RKAHPVTNAI
DGSERWWQSP PLSSGTQYNR VNLTLDLGQL FHVAYILIKF ANSPRPDLWV LERSVDFGST
YSPWQYFAHS KVDCLKEFGR EANMAVTRDD DVLCVTEYSR IVPLENGEVV VSLINGRPGA
KNFTFSHTLR EFTKATNIRL RFLRTNTLLG HLISKAQRDP TVTRRYYYSI KDISIGGQCV
CNGHAEVCNI NNPEKLFRCE CQHHTCGETC DRCCTGYNQR RWRPAAWEQS HECEACNCHG
HASNCYYDPD VERQQASLNT QGIYAGGGVC INCQHNTAGV NCEQCAKGYY RPYGVPVDAP
DGCIPCSCDP EHADGCEQGS GRCHCKPNFH GDNCEKCAIG YYNFPFCLRI PIFPVSTPSS
EDPVAGDIKG CDCNLEGVLP EICDAHGRCL CRPGVEGPRC DTCRSGFYSF PICQACWCSA
LGSYQMPCSS VTGQCECRPG VTGQRCDRCL SGAYDFPHCQ GSSSACDPAG TINSNLGYCQ
CKLHVEGPTC SRCKLLYWNL DKENPSGCSE CKCHKAGTVS GTGECRQGDG DCHCKSHVGG
DSCDTCEDGY FALEKSNYFG CQGCQCDIGG ALSSMCSGPS GVCQCREHVV GKVCQRPENN
YYFPDLHHMK YEIEDGSTPN GRDLRFGFDP LAFPEFSWRG YAQMTSVQND VRITLNVGKS
SGSLFRVILR YVNPGTEAVS GHITIYPSWG AAQSKEIIFL PSKEPAFVTV PGNGFADPFS
ITPGIWVACI KAEGVLLDYL VLLPRDYYEA SVLQLPVTEP CAYAGPPQEN CLLYQHLPVT
RFPCTLACEA RHFLLDGEPR PVAVRQPTPA HPVMVDLSGR EVELHLRLRI PQVGHYVVVV
EYSTEAAQLF VVDVNVKSSG SVLAGQVNIY SCNYSVLCRS AVIDHMSRIA MYELLADADI
QLKGHMARFL LHQVCIIPIE EFSAEYVRPQ VHCIASYGRF VNQSATCVSL AHETPPTALI
LDVLSGRPFP HLPQQSSPSV DVLPGVTLKA PQNQVTLRGR VPHLGRYVFV IHFYQAAHPT
FPAQVSVDGG WPRAGSFHAS FCPHVLGCRD QVIAEGQIEF DISEPEVAAT VKVPEGKSLV
LVRVLVVPAE NYDYQILHKK SMDKSLEFIT NCGKNSFYLD PQTASRFCKN SARSLVAFYH
KGALPCECHP TGATGPHCSP EGGQCPCQPN VIGRQCTRCA TGHYGFPRCK PCSCGRRLCE
EMTGQCRCPP RTVRPQCEVC ETHSFSFHPM AGCEGCNCSR RGTIEAAMPE CDRDSGQCRC
KPRITGRQCD RCASGFYRFP ECVPCNCNRD GTEPGVCDPG TGACLCKENV EGTECNVCRE
GSFHLDPANL KGCTSCFCFG VNNQCHSSHK RRTKFVDMLG WHLETADRVD IPVSFNPGSN
SMVADLQELP ATIHSASWVA PTSYLGDKVS SYGGYLTYQA KSFGLPGDMV LLEKKPDVQL
TGQHMSIIYE ETNTPRPDRL HHGRVHVVEG NFRHASSRAP VSREELMTVL SRLADVRIQG
LYFTETQRLT LSEVGLEEAS DTGSGRIALA VEICACPPAY AGDSCQGCSP GYYRDHKGLY
TGRCVPCNCN GHSNQCQDGS GICVNCQHNT AGEHCERCQE GYYGNAVHGS CRACPCPHTN
SFATGCVVNG GDVRCSCKAG YTGTQCERCA PGYFGNPQKF GGSCQPCSCN SNGQLGSCHP
LTGDCINQEP KDSSPAEECD DCDSCVMTLL NDLATMGEQL RLVKSQLQGL SASAGLLEQM
RHMETQAKDL RNQLLNYRSA ISNHGSKIEG LERELTDLNQ EFETLQEKAQ VNSRKAQTLN
NNVNRATQSA KELDVKIKNV IRNVHILLKQ ISGTDGEGNN VPSGDFSREW AEAQRMMREL
RNRNFGKHLR EAEADKRESQ LLLNRIRTWQ KTHQGENNGL ANSIRDSLNE YEAKLSDLRA
RLQEAAAQAK QANGLNQENE RALGAIQRQV KEINSLQSDF TKYLTTADSS LLQTNIALQL
MEKSQKEYEK LAASLNEARQ ELSDKVRELS RSAGKTSLVE EAEKHARSLQ ELAKQLEEIK
RNASGDELVR CAVDAATAYE NILNAIKAAE DAANRAASAS ESALQTVIKE DLPRKAKTLS
SNSDKLLNEA KMTQKKLKQE VSPALNNLQQ TLNIVTVQKE VIDTNLTTLR DGLHGIQRGD
IDAMISSAKS MVRKANDITD EVLDGLNPIQ TDVERIKDTY GRTQNEDFKK ALTDADNSVN
KLTNKLPDLW RKIESINQQL LPLGNISDNM DRIRELIQQA RDAASKVAVP MRFNGKSGVE
VRLPNDLEDL KGYTSLSLFL QRPNSRENGG TENMFVMYLG NKDASRDYIG MAVVDGQLTC
VYNLGDREAE LQVDQILTKS ETKEAVMDRV KFQRIYQFAR LNYTKGATSS KPETPGVYDM
DGRNSNTLLN LDPENVVFYV GGYPPDFKLP SRLSFPPYKG CIELDDLNEN VLSLYNFKKT
FNLNTTEVEP CRRRKEESDK NYFEGTGYAR VPTQPHAPIP TFGQTIQTTV DRGLLFFAEN
GDRFISLNIE DGKLMVRYKL NSELPKERGV GDAINNGRDH SIQIKIGKLQ KRMWINVDVQ
NTIIDGEVFD FSTYYLGGIP IAIRERFNIS TPAFRGCMKN LKKTSGVVRL NDTVGVTKKC
SEDWKLVRSA SFSRGGQLSF TDLGLPPTDH LQASFGFQTF QPSGILLDHQ TWTRNLQVTL
EDGYIELSTS DSGGPIFKSP QTYMDGLLHY VSVISDNSGL RLLIDDQLLR NSKRLKHISS
SRQSLRLGGS NFEGCISNVF VQRLSLSPEV LDLTSNSLKR DVSLGGCSLN KPPFLMLLKG
STRFNKTKTF RINQLLQDTP VASPRSVKVW QDACSPLPKT QANHGALQFG DIPTSHLLFK
LPQELLKPRS QFAVDMQTTS SRGLVFHTGT KNSFMALYLS KGRLVFALGT DGKKLRIKSK
EKCNDGKWHT VVFGHDGEKG RLVVDGLRAR EGSLPGNSTI SIRAPVYLGS PPSGKPKSLP
TNSFVGCLKN FQLDSKPLYT PSSSFGVSSC LGGPLEKGIY FSEEGGHVVL AHSVLLGPEF
KLVFSIRPRS LTGILIHIGS QPGKHLCVYL EAGKVTASMD SGAGGTSTSV TPKQSLCDGQ
WHSVAVTIKQ HILHLELDTD SSYTAGQIPF PPASTQEPLH LGGAPANLTT LRIPVWKSFF
GCLRNIHVNH IPVPVTEALE VQGPVSLNGC PDQ
